Prolyl isomerase Pin1 enhances osteoblast differentiation through Runx2 regulation

Sung Ho Lee, You Hee Choi, Yeon Jin Kim, Hong Seok Choi, Chang Yeol Yeo, Kwang Youl Lee

Research output: Contribution to journalArticlepeer-review

14 Scopus citations


Peptidyl-prolyl isomerase 1 (Pin1) is the only enzyme known to catalyze isomerization of the pSer/Thr-Pro peptide bond. Pin1 induces conformational change of substrates and subsequently regulates diverse cellular processes. However, its role in osteoblast differentiation is not well understood. Here we show that Pin1 enhances osteoblast differentiation. Pin1 interacts and affects the protein stability and transcriptional activity of an important osteogenic transcriptional factor Runx2. Our results indicate that this regulation is likely due to suppression of poly-ubiquitination-mediated proteasomal degradation of Runx2. Our current finding suggests that Pin1 is a novel regulator of osteoblast differentiation that acts through the regulation of Runx2 function.

Original languageEnglish
Pages (from-to)3640-3647
Number of pages8
JournalFEBS Letters
Issue number22
StatePublished - 15 Nov 2013

Bibliographical note

Funding Information:
This work is supported by the National Research Foundation of Korea (NRF) grants funded by the Korea government (MSIP) to C.-Y.Y. (No. 2012R1A5A1048236 ) and K.Y.L. ( 2011-0022259 ).


  • Osteoblast differentiation
  • Pin1
  • Runx2


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